scholarly journals Arabidopsis ATG8-INTERACTING PROTEIN1 Is Involved in Autophagy-Dependent Vesicular Trafficking of Plastid Proteins to the Vacuole

2014 ◽  
Vol 26 (10) ◽  
pp. 4084-4101 ◽  
Author(s):  
Simon Michaeli ◽  
Arik Honig ◽  
Hanna Levanony ◽  
Hadas Peled-Zehavi ◽  
Gad Galili
Keyword(s):  
Vesicular Trafficking ◽  
Plastid Proteins

scholarly journals Genome communication in plants mediated by organelle–n­ucleus-located proteins

2020 ◽  
Vol 375 (1801) ◽  
pp. 20190397 ◽  
Author(s):  
Karin Krupinska ◽  
Nicolás E. Blanco ◽  
Svenja Oetke ◽  
Michela Zottini
Keyword(s):  
Chloroplast Development ◽  
Cell Cycle Control ◽  
Plastid Transformation ◽  
Light Responses ◽  
Dual Targeting ◽  
Dual Localization ◽  
Retrograde Signalling ◽  
Eukaryotic Proteins ◽  
Plastid Proteins ◽  
Associated Proteins

An increasing number of eukaryotic proteins have been shown to have a dual localization in the DNA-containing organelles, mitochondria and plastids, and/or the nucleus. Regulation of dual targeting and relocation of proteins from organelles to the nucleus offer the most direct means for communication between organelles as well as organelles and nucleus. Most of the mitochondrial proteins of animals have functions in DNA repair and gene expression by modelling of nucleoid architecture and/or chromatin. In plants, such proteins can affect replication and early development. Most plastid proteins with a confirmed or predicted second location in the nucleus are associated with the prokaryotic core RNA polymerase and are required for chloroplast development and light responses. Few plastid–nucleus-located proteins are involved in pathogen defence and cell cycle control. For three proteins, it has been clearly shown that they are first targeted to the organelle and then relocated to the nucleus, i.e. the nucleoid-associated proteins HEMERA and Whirly1 and the stroma-located defence protein NRIP1. Relocation to the nucleus can be experimentally demonstrated by plastid transformation leading to the synthesis of proteins with a tag that enables their detection in the nucleus or by fusions with fluoroproteins in different experimental set-ups. This article is part of the theme issue ‘Retrograde signalling from endosymbiotic organelles’.

scholarly journals Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Jiqing Du ◽  
Marie-Kristin von Wrisberg ◽  
Burak Gulen ◽  
Matthias Stahl ◽  
Christian Pett ◽  
...  
Keyword(s):  
Legionella Pneumophila ◽  
Adenosine Monophosphate ◽  
Vesicular Trafficking ◽  
Bacterial Protein ◽  
Post Translational Modification ◽  
Allosteric Control ◽  
Rab Protein ◽  
Biochemical Characterisation ◽  
A Site ◽  
Insight Into

AbstractLegionella pneumophila infects eukaryotic cells by forming a replicative organelle – the Legionella containing vacuole. During this process, the bacterial protein DrrA/SidM is secreted and manipulates the activity and post-translational modification (PTM) states of the vesicular trafficking regulator Rab1. As a result, Rab1 is modified with an adenosine monophosphate (AMP), and this process is referred to as AMPylation. Here, we use a chemical approach to stabilise low-affinity Rab:DrrA complexes in a site-specific manner to gain insight into the molecular basis of the interaction between the Rab protein and the AMPylation domain of DrrA. The crystal structure of the Rab:DrrA complex reveals a previously unknown non-conventional Rab-binding site (NC-RBS). Biochemical characterisation demonstrates allosteric stimulation of the AMPylation activity of DrrA via Rab binding to the NC-RBS. We speculate that allosteric control of DrrA could in principle prevent random and potentially cytotoxic AMPylation in the host, thereby perhaps ensuring efficient infection by Legionella.

scholarly journals High Content Study of Vesicular Trafficking in Polarized Cells

2012 ◽  
Vol 102 (3) ◽  
pp. 194a
Author(s):  
Javier Mazzaferri ◽  
Stephane Lefrançois ◽  
Santiago Costantino
Keyword(s):  
Vesicular Trafficking ◽  
Polarized Cells

Analyses of Proteins Involved in Vesicular Trafficking in Platelets of Mouse Models of Hermansky Pudlak Syndrome

1999 ◽  
Vol 68 (1) ◽  
pp. 14-23 ◽  
Author(s):  
Beverly Richards-Smith ◽  
Edward K. Novak ◽  
Elliott K. Jang ◽  
Ping He ◽  
Richard J. Haslam ◽  
...  
Keyword(s):  
Mouse Models ◽  
Vesicular Trafficking ◽  
Hermansky Pudlak Syndrome

scholarly journals Vesicular trafficking in characean green algae and the possible involvement of a VAMP72-family protein

2014 ◽  
Vol 9 (4) ◽  
pp. e28466 ◽  
Author(s):  
Marion C Hoepflinger ◽  
Christina Hametner ◽  
Takashi Ueda ◽  
Ilse Foissner
Keyword(s):  
Green Algae ◽  
Vesicular Trafficking ◽  
Family Protein

The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER

1979 ◽  
Vol 35 (1) ◽  
pp. 253-266
Author(s):  
S.P. Gibbs
Keyword(s):  
Protein Synthesis ◽  
Nuclear Envelope ◽  
Outer Membrane ◽  
Chloroplast Envelope ◽  
Inhibit Protein Synthesis ◽  
Ochromonas Danica ◽  
Plastid Proteins ◽  
Regular Network ◽  
Cytoplasmic Ribosomes ◽  
Plastid Ribosomes

In 8 classes of algae, namely the Cryptophyceae, Raphidophyceae, Haptophyceae, Chrysophyceae, Bacillariophyceae, Xanthophyceae, Eustigmatophyceae and Phaeophyceae, the chloroplasts, in addition to being surrounded by a double-membraned chloroplast envelope, are also enclosed by a cisterna of endoplasmic reticulum called the chloroplast ER. Often this ER cisterna is continuous with the outher membrane of the nuclear envelope in such a manner that the nuclear envelope forms a part of the ER sac enclosing the chloroplast. In all these classes of algae except the Cryptophyceae, a regular network of tubules and vesicles, named the periplastidal reticulum, is present at a specific location between the chloroplast envelope and the chloroplast ER. In the Cryptophyceae, scattered vesicles are found between the chloroplast envelope and the chloroplast ER. Ribosomes which have been shown to be arranged to polysomes are found on the outer membrane of the chloroplast ER. It is proposed that nuclear-coded proteins which are destined for the chloroplast are synthesized on these polysomes, passing during synthesis into the lumen of the ER cisterna. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles then fuse with the outer membrane of the chloroplast envelope thereby delivering their contents to the lumen of the chloroplast envelope. Proteins then cross the inner membrane of the chloroplast envelope in an as yet unknown manner. Experimental evidence for this hypothesis comes from studies on Ochromonas danica using chloramphenicol and spectinomycin, which inhibit protein synthesis on plastid ribosomes, and cycloheximide, which inhibits protein synthesis on cytoplasmic ribosomes. In cells of Ochromonas exposed to chloramphenicol or spectinomycin, the periplastidal reticulum proliferates markedly becoming several layers thick. Presumably this build up of periplastidal reticulum occurs because the transport of cytoplasmically synthesized plastid proteins is slowed down when protein synthesis in the chloroplast is inhibited. Conversely, when cells of Ochromonas are treated with cycloheximide, there is a reduction in the amount of periplastidal reticulum presumably because there are no cytoplasmically synthesized proteins to be transported into the chloroplast.

Organization of vesicular trafficking in epithelia

2005 ◽  
Vol 6 (3) ◽  
pp. 233-247 ◽  
Author(s):  
Enrique Rodriguez-Boulan ◽  
Geri Kreitzer ◽  
Anne Müsch
Keyword(s):  
Vesicular Trafficking

scholarly journals Retromer has a selective function in cargo sorting via endosome transport carriers

2018 ◽  
Vol 218 (2) ◽  
pp. 615-631 ◽  
Author(s):  
Yi Cui ◽  
Julian M. Carosi ◽  
Zhe Yang ◽  
Nicholas Ariotti ◽  
Markus C. Kerr ◽  
...  
Keyword(s):  
Vesicular Trafficking ◽  
Lysosomal Hydrolases ◽  
Cell Level ◽  
Ultrastructural Alteration ◽  
Membrane Protein Complex ◽  
Lysosomal Function ◽  
Trafficking Pathway ◽  
Peripheral Membrane Protein ◽  
And Function ◽  
Proteolytic Capacity

Retromer is a peripheral membrane protein complex that coordinates multiple vesicular trafficking events within the endolysosomal system. Here, we demonstrate that retromer is required for the maintenance of normal lysosomal morphology and function. The knockout of retromer subunit Vps35 causes an ultrastructural alteration in lysosomal structure and aberrant lysosome function, leading to impaired autophagy. At the whole-cell level, knockout of retromer Vps35 subunit reduces lysosomal proteolytic capacity as a consequence of the improper processing of lysosomal hydrolases, which is dependent on the trafficking of the cation-independent mannose 6-phosphate receptor (CI-M6PR). Incorporation of CI-M6PR into endosome transport carriers via a retromer-dependent process is restricted to those tethered by GCC88 but not golgin-97 or golgin-245. Finally, we show that this retromer-dependent retrograde cargo trafficking pathway requires SNX3, but not other retromer-associated cargo binding proteins, such as SNX27 or SNX-BAR proteins. Therefore, retromer does contribute to the retrograde trafficking of CI-M6PR required for maturation of lysosomal hydrolases and lysosomal function.

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